And that’s a wrap!

There we have it, Crispr and lithium-ion batteries lose out to cryo-electron microscopy, a technique that has allowed scientists to study molecules in unprecedented resolution – an advance that could help with drug discovery and fundamental understanding of biological processes.

Congratulations to the three winners Jacques Dubochet, Joachim Frank and Richard Henderson.

“It shows the value of patiently supporting basic science for decades,” he says. But, he adds, what started in basic science has led to incredible revelations. “By the time it has got to this stage, it’s already being used by drug companies to do structures of important drug targets, and it is used to understand fundamental biology that can change medicine in the future- so it just goes to show you how all these things are linked.”

Those who contest that the winners have taken the prize for biochemistry, rather than chemistry, here’s a fun fact: 50 of those who have scooped the award actually work(ed) in biochemistry, making it the most common field for laureates of this prize.

Here’s a description of the prize-winning work from the Nobel committee:

A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery. Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure.

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

While this year’s laureates are worthy winners, they haven’t broken the record for age: the youngest chemistry laureate remains Frédéric Joliot, Marie Curie’s son-in-law, who shared the prize with his wife, Irene, in 1935. Joliot was 35.

John Hardy, professor of neuroscience at University College London, said that cryo-electron microscopy has also proven valuable in unpicking the structure of the enzyme that produces amyloid proteins that are involved in Alzheimer’s disease. That, he adds, could aid the design of drugs to tackle the disease.

“And as a biologist, I can say that the pictures are beautiful,” he said.

Dr Carsten Sachse, of the European Molecular Biology Laboratory used to work with Richard Henderson at the MRC Laboratory of Molecular Biology, Cambridge. He tells the Guardian that Henderson was an inspiring person to work with.

“He was really visionary, he saw it all coming. When I worked with him, that was a time when it was not clear how far the technology really would go, but he had it all worked out in his head,” said Sachse.

Reaction continues to come in. Magdalena Zernicka-Goetz, professor of mammalian development and stem cell biology at the University of Cambridge, said that she thought the win was wonderful. “A visual image is the essential component to understanding, often the first one to open our eyes – and so our minds – to a scientific breakthrough.”

Dame Athene Donald, professor of experimental physics at the University of Cambridge said that cryo-electron microscopy has made a huge difference, allowing biological molecules to be studied at extremely high resolution.

“The only talk I remember from the first electron microscopy conference I attended during my PhD was by Nigel Unwin and Richard Henderson on purple membrane. It was stunning work. It’s a long time ago but it’s brilliant to see the developments finally be rewarded by this year’s award,” she said.

Joachim Frank tells the press conference that the coolest molecules he has seen using the technique of cryo-electron microscopy are ribosomes, the protein factories of cells. The technique, he says, has allowed scientists to explore the details of how amino acids are put together to form proteins.

Barry Fuller, professor in surgical sciences at University College London Medical School, said that it was important not to get confused by the “cryo” side of the work, and that it was not directly linked to efforts to preserve cells and tissues.

While the molecules are “frozen in time”, he noted, there is no ice or antifreeze involved – instead the technique uses ultra-ultrafast cooling.

“But to turn this on its head, understanding configurations and stability of biomolecules at cryogenic temperatures will always improve the efforts of cryobiolgy,” he said.

More reaction: Dame Carol Robinson, professor of chemistry at the Oxford University, described cryo-electron microscopy as “transformative” in allowing scientists to see new images of important biological molecules.

“I am personally very happy for Richard, who predicted this would be possible many years previously,” she said.